2btw
From Proteopedia
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| - | [[Image:2btw.gif|left|200px]] | + | [[Image:2btw.gif|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF ALR0975''' | + | {{Structure |
| + | |PDB= 2btw |SIZE=350|CAPTION= <scene name='initialview01'>2btw</scene>, resolution 2.00Å | ||
| + | |SITE= <scene name='pdbsite=AC1:Ca+Binding+Site+For+Chain+B'>AC1</scene> | ||
| + | |LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Glutathione_gamma-glutamylcysteinyltransferase Glutathione gamma-glutamylcysteinyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.2.15 2.3.2.15] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CRYSTAL STRUCTURE OF ALR0975''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2BTW is a [ | + | 2BTW is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Anabaena_sp. Anabaena sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BTW OCA]. |
==Reference== | ==Reference== | ||
| - | A papain-like enzyme at work: native and acyl-enzyme intermediate structures in phytochelatin synthesis., Vivares D, Arnoux P, Pignol D, Proc Natl Acad Sci U S A. 2005 Dec 27;102(52):18848-53. Epub 2005 Dec 9. PMID:[http:// | + | A papain-like enzyme at work: native and acyl-enzyme intermediate structures in phytochelatin synthesis., Vivares D, Arnoux P, Pignol D, Proc Natl Acad Sci U S A. 2005 Dec 27;102(52):18848-53. Epub 2005 Dec 9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16339904 16339904] |
[[Category: Anabaena sp.]] | [[Category: Anabaena sp.]] | ||
[[Category: Glutathione gamma-glutamylcysteinyltransferase]] | [[Category: Glutathione gamma-glutamylcysteinyltransferase]] | ||
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[[Category: glutathione metabolism]] | [[Category: glutathione metabolism]] | ||
[[Category: nostoc]] | [[Category: nostoc]] | ||
| - | [[Category: | + | [[Category: pc]] |
[[Category: phytochelatin synthase]] | [[Category: phytochelatin synthase]] | ||
[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:06:40 2008'' |
Revision as of 14:06, 20 March 2008
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| , resolution 2.00Å | |||||||
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| Sites: | |||||||
| Ligands: | |||||||
| Activity: | Glutathione gamma-glutamylcysteinyltransferase, with EC number 2.3.2.15 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF ALR0975
Overview
Phytochelatin synthase (PCS) is a key enzyme for heavy-metal detoxification in plants. PCS catalyzes the production of glutathione (GSH)-derived peptides (called phytochelatins or PCs) that bind heavy-metal ions before vacuolar sequestration. The enzyme can also hydrolyze GSH and GS-conjugated xenobiotics. In the cyanobacterium Nostoc, the enzyme (NsPCS) contains only the catalytic domain of the eukaryotic synthase and can act as a GSH hydrolase and weakly as a peptide ligase. The crystal structure of NsPCS in its native form solved at a 2.0-A resolution shows that NsPCS is a dimer that belongs to the papain superfamily of cysteine proteases, with a conserved catalytic machinery. Moreover, the structure of the protein solved as a complex with GSH at a 1.4-A resolution reveals a gamma-glutamyl cysteine acyl-enzyme intermediate stabilized in a cavity of the protein adjacent to a second putative GSH binding site. GSH hydrolase and PCS activities of the enzyme are discussed in the light of both structures.
About this Structure
2BTW is a Protein complex structure of sequences from Anabaena sp.. Full crystallographic information is available from OCA.
Reference
A papain-like enzyme at work: native and acyl-enzyme intermediate structures in phytochelatin synthesis., Vivares D, Arnoux P, Pignol D, Proc Natl Acad Sci U S A. 2005 Dec 27;102(52):18848-53. Epub 2005 Dec 9. PMID:16339904
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